Structural highlights
Function
MEPS_ECOLI A murein DD-endopeptidase with specificity for D-Ala-meso-diaminopimelic acid (mDAP) cross-links. Its role is probably to cleave D-Ala-mDAP cross-links to allow insertion of new glycans and thus cell wall expansion. Functionally redundant with MepM and MepH. Also has weak LD-carboxypeptidase activity on L-mDAP-D-Ala peptide bonds. Partially suppresses a prc disruption mutant.[1] [2]
References
- ↑ Singh SK, SaiSree L, Amrutha RN, Reddy M. Three redundant murein endopeptidases catalyse an essential cleavage step in peptidoglycan synthesis of Escherichia coli K12. Mol Microbiol. 2012 Dec;86(5):1036-51. PMID:23062283 doi:10.1111/mmi.12058
- ↑ Hara H, Abe N, Nakakouji M, Nishimura Y, Horiuchi K. Overproduction of penicillin-binding protein 7 suppresses thermosensitive growth defect at low osmolarity due to an spr mutation of Escherichia coli. Microb Drug Resist. 1996 Spring;2(1):63-72. PMID:9158724 doi:10.1089/mdr.1996.2.63
